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PDBsum entry 1cp6
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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1-Butaneboronic acid binding to aeromonas proteolytica aminopeptidase: a case of arrested development.
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Authors
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C.C.De paola,
B.Bennett,
R.C.Holz,
D.Ringe,
G.A.Petsko.
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Ref.
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Biochemistry, 1999,
38,
9048-9053.
[DOI no: ]
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PubMed id
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Abstract
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Hydrolases containing two metal ions connected by a bridging ligand catalyze
reactions important in carcinogensis, tissue repair, post-translational
modification, control and regulation of biochemical pathways, and protein
degradation. The aminopeptidase from Aeromonas proteolytica serves as a paradigm
for the study of such bridged bimetallic proteases since its three-dimensional
structure is known to very high resolution and its catalytic reaction is
amenable to spectroscopic examination. Herein, we report the X-ray crystal
structure at 1.9 A resolution of AAP complexed with 1-butaneboronic acid (BuBA).
This structure suggests that this complex represents a snapshot of the
proteolytic reaction in an arrested form between the Michaelis complex and the
transition state. Comparison of the structure with spectroscopic and other data
allows us to conclude that the apparently structurally symmetrical dizinc site
is actually asymmetric electrostatically.
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Secondary reference #1
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Title
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Crystal structure of aeromonas proteolytica aminopeptidase: a prototypical member of the co-Catalytic zinc enzyme family.
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Authors
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B.Chevrier,
C.Schalk,
H.D'Orchymont,
J.M.Rondeau,
D.Moras,
C.Tarnus.
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Ref.
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Structure, 1994,
2,
283-291.
[DOI no: ]
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PubMed id
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Figure 3.
Figure 3. (a) Stereoview of the zinc ligands in the
metal-binding site. Dashed lines indicate the strong
zinc–ligand interactions. (b) Stereoview of the electron
density contoured at 1.5 σ level. This view emphasizes the
bidendate character of the Zn2– carboxylate interaction with
Asp179. A similar interaction is observed between Glu152 (not
labeled) and Zn1. Figure 3. (a) Stereoview of the zinc
ligands in the metal-binding site. Dashed lines indicate the
strong zinc–ligand interactions. (b) Stereoview of the
electron density contoured at 1.5 σ level. This view emphasizes
the bidendate character of the Zn2– carboxylate interaction
with Asp179. A similar interaction is observed between Glu152
(not labeled) and Zn1.
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Figure 7.
Figure 7. Histogram plotting the number of water molecules with
respect to their distance from the closest polar protein atoms.
Figure 7. Histogram plotting the number of water molecules
with respect to their distance from the closest polar protein
atoms.
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The above figures are
reproduced from the cited reference
with permission from Cell Press
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